Thermal denaturation of porcine myofibrillar proteins at different heating temperatures: A focus on the surface hydrophobicity
Year: 2025
Type: article
Abstract: Changes in the hydrophobic interactions of porcine myofibrillar proteins (MPs) were investigated at various heating and internal temperatures (ITs). MP extracts were heated at 50, 60, 70, 80, or 90 °C until their ITs reached the same respective values (±2 °C) and were labeled IT50, IT60, IT70, IT80, and IT90. The intrinsic tryptophan fluorescence intensity (FI) of the MPs decreased after heating at all ITs ( P < 0.05). FI max decreased significantly between IT50 and IT60 ( P < 0.05) and increased from IT70 onward ( P > 0.05), with IT80 and IT90 exhibiting higher FIs than IT60 ( P < 0.05). Surface hydrophobicity increased at IT50 ( P < 0.05), decreased at IT60 (P < 0.05), and peaked at IT80-IT90 (P < 0.05), compared with unheated MP. Fluorescence and confocal laser scanning microscopy images revealed a considerable aggregation increase from IT60, with notable exposure of the non-polar regions at IT60-IT90. Consequently, increased surface hydrophobicity remained even after MP coagulation when IT exceeded the myosin denaturation temperature. • Hydrophobic interaction changes in MPs were studied at various ITs after heating. • Intrinsic tryptophan FI max of MPs decreased by heating with the shifts in λ max . • Aggregation considerably increased from IT60, exposing more nonpolar regions. • Surface hydrophobicity remained high even after the heat-induced MP coagulation.
Source: Food Chemistry X
Institutions: Korea Food Research Institute, Chungnam National University
Language: English
Subfield: Animal Science and Zoology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,330
Award: G1049688542
OpenAlex ID: W4413120965